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An S-layer (surface layer) is a cell surface protein layer found in many different bacteria and in some archaea, where it serves as the cell wall. All S-layers are made up of a two-dimensional array of proteins and have a crystalline appearance, the symmetry of which differs between species.
Protein A is a 42 kDa surface protein originally found in the cell wall of the bacteria Staphylococcus aureus. It is encoded by the spa gene and its regulation is controlled by DNA topology, cellular osmolarity, and a two-component system called ArlS-ArlR. It has found use in biochemical research because of its ability to bind immunoglobulins ...
Lipopolysaccharides can have substantial impacts on human health, primarily through interactions with the immune system. LPS is a potent activator of the immune system and is a pyrogen (agent that causes fever). [4] In severe cases, LPS can trigger a brisk host response and multiple types of acute organ failure [5] which can lead to septic ...
The other proteins are EsaA, EssB, EssA, that are membrane proteins that function alongside EssC to mediate protein secretion. The exact mechanism of how substrates reach the cell surface is unknown, as is the interaction of the three membrane proteins with each other and EssC.
An S-layer (surface layer) is a part of the cell envelope found in almost all archaea, as well as in many types of bacteria. [1] [2] The S-layers of both archaea and bacteria consists of a monomolecular layer composed of only one (or, in a few cases, two) identical proteins or glycoproteins. [3]
FimH is a bacterial adhesin that helps bacteria such as Escherichia coli to bind to host cells and their receptors (here: the human proteins CD48 and TLR4, or mannose residues). [ 4 ] Most fimbria of gram-negative bacteria function as adhesins, but in many cases it is a minor subunit protein at the tip of the fimbriae that is the actual adhesin.
Virulence-related outer membrane proteins, or outer surface proteins (Osp) in some contexts, are expressed in the outer membrane of gram-negative bacteria and are essential to bacterial survival within macrophages and for eukaryotic cell invasion. This family consists of several bacterial and phage Ail/Lom-like proteins.
Internalins are surface proteins found on Listeria monocytogenes. They exist in two known forms, InlA and InlB. They are used by the bacteria to invade mammalian cells via cadherins transmembrane proteins and Met receptors respectively. The exact role of these proteins and their invasiveness in vivo is not completely understood.